Metal-catalyzed oxidation induces carbonylation of peroxisomal proteins and loss of enzymatic activities

Nguyen, AnhThu; Donaldson, Robert P.

doi:10.1016/j.abb.2005.04.018

Cited by 77 publications

(48 citation statements)

References 27 publications

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“…In particular, the activity of the key glyoxylate cycle enzyme isocitrate lyase (Eastmond et al, 2000a) is reduced by 80% in the strongest catalase antisense line. This observation is consistent with recent in vitro data, which show that isocitrate lyase from castor bean (Ricinus communis) endosperm is readily inactivated by H 2 O 2 and that this enzyme physically associates with catalase in the peroxisome (Nguyen and Donaldson, 2005;Yanik and Donaldson, 2005).…”

Section: Discussionsupporting

confidence: 82%

“…The only modification to the method was that the lipids were extracted from oil bodies in 1.5-mL tubes without homogenization. The levels of protein carbonyls in oil body membranes and purified recombinant SDP1 were determined using the spectrophotometric quantification method described by Nguyen and Donaldson (2005). SDP1 was immunoprecipitated from oil body membranes using the IP50 Protein G Immunoprecipitation kit (Sigma-Aldrich), and carbonyl groups were detected using the OxyBlot protein oxidation detection kit (Millipore) as described by Nguyen and Donaldson (2005).…”

Section: Microscopymentioning

confidence: 99%

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MONODEHYROASCORBATE REDUCTASE4 Is Required for Seed Storage Oil Hydrolysis and Postgerminative Growth in Arabidopsis

Eastmond

2007

The Plant Cell

106

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Hydrogen peroxide is a major by-product of peroxisomal metabolism and has the potential to cause critical oxidative damage. In all eukaryotes, catalase is thought to be instrumental in removing this H2O2. However, plants also contain a peroxisomal membrane–associated ascorbate-dependent electron transfer system, using ascorbate peroxidase and monodehydroascorbate reductase (MDAR). Here, I report that the conditional seedling-lethal sugar-dependent2 mutant of Arabidopsis thaliana is deficient in the peroxisomal membrane isoform of MDAR (MDAR4). Following germination, Arabidopsis seeds rely on storage oil breakdown to supply carbon skeletons and energy for early seedling growth, and massive amounts of H2O2 are generated within the peroxisome as a by-product of fatty acid β-oxidation. My data suggest that the membrane-bound MDAR4 component of the ascorbate-dependent electron transfer system is necessary to detoxify H2O2, which escapes the peroxisome. This function appears to be critical to protect oil bodies that are in close proximity to peroxisomes from incurring oxidative damage, which otherwise inactivates the triacylglycerol lipase SUGAR-DEPENDENT1 and cuts off the supply of carbon for seedling establishment.

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Section: Discussionsupporting

confidence: 82%

Section: Microscopymentioning

confidence: 99%

MONODEHYROASCORBATE REDUCTASE4 Is Required for Seed Storage Oil Hydrolysis and Postgerminative Growth in Arabidopsis

Eastmond

2007

The Plant Cell

106

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“…In support of this, studies in castor bean (Ricinus communis) peroxisomal proteins have also demonstrated a lack of correlation between the extent of protein oxidation and the inhibition of protein function following MCO (Nguyen and Donaldson, 2005). The prospect of having to perform functional analysis on all oxidized proteins to infer effects is daunting.…”

Section: +mentioning

confidence: 90%

Divalent Metal Ions in Plant Mitochondria and Their Role in Interactions with Proteins and Oxidative Stress-Induced Damage to Respiratory Function

et al. 2009

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Understanding the metal ion content of plant mitochondria and metal ion interactions with the proteome are vital for insights into both normal respiratory function and the process of protein damage during oxidative stress. We have analyzed the metal content of isolated Arabidopsis (Arabidopsis thaliana) mitochondria, revealing a 26:8:6:1 molar ratio for iron:zinc:copper: manganese and trace amounts of cobalt and molybdenum. We show that selective changes occur in mitochondrial copper and iron content following in vivo and in vitro oxidative stresses. Immobilized metal affinity chromatography charged with Cu 2+ , Zn 2+ , and Co 2+ was used to identify over 100 mitochondrial proteins with metal-binding properties. There were strong correlations between the sets of immobilized metal affinity chromatography-interacting proteins, proteins predicted to contain metal-binding motifs, and protein sets known to be oxidized or degraded during abiotic stress. Mitochondrial respiratory chain pathways and matrix enzymes varied widely in their susceptibility to metal-induced loss of function, showing the selectivity of the process. A detailed study of oxidized residues and predicted metal interaction sites in the tricarboxylic acid cycle enzyme aconitase identified selective oxidation of residues in the active site and showed an approach for broader screening of functionally significant oxidation events in the mitochondrial proteome.

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“…Varying degrees of activity loss were detected in a number of peroxisomal enzymes following metal-catalysedinduced carbonylation [50]. The formation of protein carbonyls by HNE adducts has been shown to have significant effects on protein function and is frequently associated with their cross-linking.…”

Section: The Impact Of Carbonylation On Protein Functionmentioning

confidence: 99%

Protein carbonylation, cellular dysfunction, and disease progression

Dalle‐Donne

Aldini

Colombo

et al. 2006

Journal of Cellular and Molecular Medicine

717

545

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Carbonylation of proteins is an irreversible oxidative damage, often leading to a loss of protein function, which is considered a widespread indicator of severe oxidative damage and disease-derived protein dysfunction. Whereas moderately carbonylated proteins are degraded by the proteasomal system, heavily carbonylated proteins tend to form high-molecular-weight aggregates that are resistant to degradation and accumulate as damaged or unfolded proteins. Such aggregates of carbonylated proteins can inhibit proteasome activity. A large number of neurodegenerative diseases are directly associated with the accumulation of proteolysis-resistant aggregates of carbonylated proteins in tissues. Identification of specific carbonylated protein(s) functionally impaired and development of selective carbonyl blockers should lead to the definitive assessment of the causative, correlative or consequential role of protein carbonylation in disease onset and/or progression, possibly providing new therapeutic aproaches.

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Metal-catalyzed oxidation induces carbonylation of peroxisomal proteins and loss of enzymatic activities

Cited by 77 publications

References 27 publications

MONODEHYROASCORBATE REDUCTASE4 Is Required for Seed Storage Oil Hydrolysis and Postgerminative Growth in Arabidopsis

MONODEHYROASCORBATE REDUCTASE4 Is Required for Seed Storage Oil Hydrolysis and Postgerminative Growth in Arabidopsis

Divalent Metal Ions in Plant Mitochondria and Their Role in Interactions with Proteins and Oxidative Stress-Induced Damage to Respiratory Function

Protein carbonylation, cellular dysfunction, and disease progression

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